| Autor: |
Boonmee, Atcha, Ruppert, Thomas, Herrmann, Richard |
| Předmět: |
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| Zdroj: |
FEMS Microbiology Letters; Jan2009, Vol. 290 Issue 2, p174-181, 8p, 3 Black and White Photographs, 1 Diagram, 1 Chart, 1 Graph |
| Abstrakt: |
The gene mpn310 from Mycoplasma pneumoniae encodes the proteins HMW2 with a molecular weight of 215 621 and the smaller P28, here called HMW2-s. Because HMW2-s is not well defined, it was isolated from protein extracts of M. pneumoniae cells and its N-terminal end was determined by MS. HMW2-s starts with the methionine at the amino acid position 1620 of HMW2 and its residual sequence is identical to the last 198 amino acids of HMW2, predicting a molecular weight of 23 204. These results were confirmed by the comparative MS analysis of HMW2-s that had been synthesized in Escherichia coli. A precursor–product relationship between HMW2 and HMW2-s could be excluded, because HMW2-s can be translated from a specific mRNA starting within mpn310. The conservation of an HMW2-s like protein in M. pneumoniae and Mycoplasma genitalium emphasizes its possible functional importance. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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